Probing temperature‐ and solvent‐dependent protein dynamics using terahertz time‐domain spectroscopy

Kasia Tych, Christopher D. Wood, Andrew D. Burnett, Arwen R. Pearson, Edmund H. Linfield, John E. Cunningham*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

3 Citations (Scopus)
7 Downloads (Pure)


The effect of temperature on the terahertz‐frequency‐range material properties of lyophilized and single‐crystal hen egg‐white lysozyme has been measured using terahertz time‐domain spectroscopy, with the results presented and discussed in the context of protein and solvent dynamical and glass transitions. Lyophilized hen egg‐white lysozyme was measured over a temperature range from 4 to 290 K, and a change in the dynamical behaviour of the sample at around 100 K was observed through a change in the terahertz absorption spectrum. Additionally, the effect of cryoprotectants on the temperature‐dependent absorption coefficient is studied, and it is demonstrated that terahertz time‐domain spectroscopy is capable of resolving the true glass transition temperature of single‐crystal hen egg‐white lysozyme at ∼150 K, which is in agreement with literature values measured using differential scanning calorimetry.
Original languageEnglish
Pages (from-to)146-153
Number of pages8
JournalJournal of Applied Crystallography
Issue number1
Publication statusPublished - Feb-2014
Externally publishedYes

Cite this